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Tytuł:
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Noncanonical scaffolding of G αi and β-arrestin by G protein-coupled receptors.
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Autorzy:
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Smith JS; Department of Medicine, Duke University Medical Center, Durham, NC 27710, USA.; Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
Pack TF; Department of Cell Biology, Duke University Medical Center, Durham, NC 27710, USA.; Department of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, NC 27710, USA.
Inoue A; Department of Pharmaceutical Sciences, Tohoku University, Japan.
Lee C; Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
Zheng K; Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
Choi I; Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
Eiger DS; Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
Warman A; Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
Xiong X; Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
Ma Z; Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
Viswanathan G; Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
Levitan IM; Department of Cell Biology, Duke University Medical Center, Durham, NC 27710, USA.
Rochelle LK; Department of Cell Biology, Duke University Medical Center, Durham, NC 27710, USA.; Department of Surgery, Duke University Medical Center, Durham, NC 27710, USA.
Staus DP; Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
Snyder JC; Department of Cell Biology, Duke University Medical Center, Durham, NC 27710, USA.; Department of Surgery, Duke University Medical Center, Durham, NC 27710, USA.
Kahsai AW; Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
Caron MG; Department of Medicine, Duke University Medical Center, Durham, NC 27710, USA.; Department of Cell Biology, Duke University Medical Center, Durham, NC 27710, USA.; Department of Neurobiology, Duke University Medical Center, Durham, NC 27710, USA.
Rajagopal S; Department of Medicine, Duke University Medical Center, Durham, NC 27710, USA. .; Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
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Źródło:
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Science (New York, N.Y.) [Science] 2021 Mar 12; Vol. 371 (6534). Date of Electronic Publication: 2021 Jan 21.
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Typ publikacji:
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Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
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Język:
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English
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Imprint Name(s):
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Publication: : Washington, DC : American Association for the Advancement of Science
Original Publication: New York, N.Y. : [s.n.] 1880-
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MeSH Terms:
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GTP-Binding Protein alpha Subunits, Gi-Go/*metabolism
Receptors, G-Protein-Coupled/*metabolism
beta-Arrestins/*metabolism
Bioluminescence Resonance Energy Transfer Techniques ; Cell Movement ; Extracellular Signal-Regulated MAP Kinases/metabolism ; HEK293 Cells ; Humans ; Signal Transduction
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References:
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Grant Information:
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K22 CA212058 United States CA NCI NIH HHS; F31 DA041160 United States DA NIDA NIH HHS; K08 HL114643 United States HL NHLBI NIH HHS; T32 GM145449 United States GM NIGMS NIH HHS; R01 GM122798 United States GM NIGMS NIH HHS; T32 GM007171 United States GM NIGMS NIH HHS; R37 MH073853 United States MH NIMH NIH HHS
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Substance Nomenclature:
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0 (Receptors, G-Protein-Coupled)
0 (beta-Arrestins)
EC 2.7.11.24 (Extracellular Signal-Regulated MAP Kinases)
EC 3.6.5.1 (GTP-Binding Protein alpha Subunits, Gi-Go)
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Entry Date(s):
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Date Created: 20210122 Date Completed: 20210330 Latest Revision: 20221019
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Update Code:
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20240105
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PubMed Central ID:
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PMC8005335
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DOI:
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10.1126/science.aay1833
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PMID:
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33479120
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Heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors (GPCRs) are common drug targets and canonically couple to specific G α protein subtypes and β-arrestin adaptor proteins. G protein-mediated signaling and β-arrestin-mediated signaling have been considered separable. We show here that GPCRs promote a direct interaction between G αi protein subtype family members and β-arrestins regardless of their canonical G α protein subtype coupling. G αi :β-arrestin complexes bound extracellular signal-regulated kinase (ERK), and their disruption impaired both ERK activation and cell migration, which is consistent with β-arrestins requiring a functional interaction with G αi for certain signaling events. These results introduce a GPCR signaling mechanism distinct from canonical G protein activation in which GPCRs cause the formation of G αi :β-arrestin signaling complexes.
(Copyright © 2021 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.)
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